Superoxide Dismutase

The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis.

Weber, K., & Osborn, M. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)94333-4 · Cited by 16,688

DISC ELECTROPHORESIS – II METHOD AND APPLICATION TO HUMAN SERUM PROTEINS *

Davis, B. J. (1964) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1964.tb14213.x · Cited by 16,129

Superoxide Dismutase

McCord, J. M., & Fridovich, I. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63504-5 · Cited by 12,952

Superoxide dismutase: Improved assays and an assay applicable to acrylamide gels

Beauchamp, C., & Fridovich, I. (1971) · Analytical Biochemistry · doi:10.1016/0003-2697(71)90370-8 · Cited by 12,892

Spectroscopic Determination of Tryptophan and Tyrosine in Proteins *

Edelhoch, H. (1967) · Biochemistry · doi:10.1021/bi00859a010 · Cited by 3,438

Equilibrium Ultracentrifugation of Dilute Solutions*

Yphantis, D. A. (1964) · Biochemistry · doi:10.1021/bi00891a003 · Cited by 3,386

High resolution acrylamide gel electrophoresis of histones

Panyim, S., & Chalkley, R. G. (1969) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(69)90042-3 · Cited by 2,459

THE OXIDATION OF RIBONUCLEASE WITH PERFORMIC ACID

Hirs, C. H. W. (1956) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)65721-7 · Cited by 1,862

ORIGIN OF EUKARYOTIC CELLS

Raven, P. H., & Margulis, L. (1971) · Evolution · doi:10.1111/j.1558-5646.1971.tb01930.x · Cited by 1,483

An Enzyme-Based Theory of Obligate Anaerobiosis: The Physiological Function of Superoxide Dismutase

McCord, J. M., Keele, B. B., & Fridovich, I. (1971) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.68.5.1024 · Cited by 976

Superoxide dismutase activity in brains from chronic alcoholics

Marklund, S. L., Oreland, L., Perdahl, E., & Winblad, B. G. (1983) · Drug and Alcohol Dependence · doi:10.1016/0376-8716(83)90062-5 · Cited by 26

Effect of superoxide dismutase on the development of preimplantation mouse embryos

Chun, Y. S., Kim, J. H., Lee, H. T., & Chung, K. S. (1994) · Theriogenology · doi:10.1016/0093-691x(94)90087-y · Cited by 26

Superoxide Dismutase (Erythrocuprein) and Free Radicals in Clinical Chemistry

Gutteridge, J. M. C. (1976) · Annals of Clinical Biochemistry International Journal of Laboratory Medicine · doi:10.1177/000456327601300125 · Cited by 26

Superoxide Dismutase Activity in Polymorphonuclear Leukocytes and Alveolar Macrophages of Protein Malnourished Rats and Guinea Pigs

WATSON, R. R., Rister, M., & Baehner, R. L. (1976) · Journal of Nutrition · doi:10.1093/jn/106.12.1801 · Cited by 26

Bush sophora root polysaccharide could help prevent aflatoxin B1-induced hepatotoxicity in the primary chicken hepatocytes

Gan, F., Yang, Y., Chen, Y., Che, C., Pan, C., & Huang, K. (2018) · Toxicon · doi:10.1016/j.toxicon.2018.05.019 · Cited by 25

Micronutrient and redox homeostasis contribute to Moringa oleifera-regulated drought tolerance in wheat

Basu, S., Prabhakar, A. A., Kumari, S., Aabha, Kumar, R. R., Shekhar, S., Prakash, K., Singh, J. P., Singh, G. P., Prasad, R., et al. (2022) · Plant Growth Regulation · doi:10.1007/s10725-022-00795-z · Cited by 25

Plant growth promoting rhizobacterium Bacillus sp. BSE01 alleviates salt toxicity in chickpea (Cicer arietinum L.) by conserving ionic, osmotic, redox and hormonal homeostasis

Basu, S., Kumari, S., Subhadarshini, P., Rishu, A. K., Shekhar, S., & Kumar, G. (2023) · Physiologia Plantarum · doi:10.1111/ppl.14076 · Cited by 25

MnSOD Protein Content Changes in Hypoxic/Hypoperfused Lung Tissue

Russell, W., & Jackson, R. M. (1993) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb/9.6.610 · Cited by 25

Oxidative stress induced in tobacco leaves by chloroplast over-expression of maize plastidial transglutaminase

Ortigosa, S. M., Díaz‐Vivancos, P., Clemente‐Moreno, M. J., Pintó‐Marijuan, M., Fleck, I., Veramendi, J., Santos, M., Hernández, J. A., & Torné, J. M. (2010) · Planta · doi:10.1007/s00425-010-1185-y · Cited by 25

Myocardial protection with endogenous overexpression of manganese superoxide dismutase

Suzuki, K., Sawa, Y., Ichikawa, H., Kaneda, Y., & Matsuda, H. (1999) · The Annals of Thoracic Surgery · doi:10.1016/s0003-4975(99)00726-2 · Cited by 25

Genetic control of the mitochondrial form of superoxide dismutase in hexaploid wheat

Neuman, P. R., & Hart, G. E. (1986) · Biochemical Genetics · doi:10.1007/bf00499098 · Cited by 25

Cellular effects of hematoporphyrin derivative photodynamic therapy on normal and neoplastic rat bladder cells.

Shulok, J. R., Klaunig, J. E., Sh, S., Schafer, P. J., & Pj, G. (1986) · PubMed Central · Cited by 25

The Control of Iron-Induced Oxidative Damage in Isolated Rat-Liver Mitochondria by Respiration State and Ascorbate

Burkitt, M. J., & Gilbert, B. C. (1989) · Free Radical Research Communications · doi:10.3109/10715768909073416 · Cited by 25

Chemical aspects of the structure, function and evolution of superoxide dismutases

Parker, M. W., Schininà, M. E., Bossa, F., & Bannister, J. V. (1984) · Inorganica Chimica Acta · doi:10.1016/s0020-1693(00)81854-x · Cited by 25

Membrane-bound glutathione peroxidase-like activity in mitochondria

Katki, A. G., & Myers, C. E. (1980) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(80)91184-5 · Cited by 25

Covalent Protein Modification: An Unignorable Factor for Bisphenol A-Induced Hepatotoxicity

Hu, X., Wu, J., Wen, M., Long, F., Pan, H., Peng, T., Yao, X., & Li, N. (2022) · Environmental Science & Technology · doi:10.1021/acs.est.2c01307 · Cited by 25

Metalloporphyrins improve the survival of Sod2‐deficient neurons

Patel, M. N. (2003) · Aging Cell · doi:10.1046/j.1474-9728.2003.00055.x · Cited by 24

Alternative system of succinate oxidation in glyoxysomes of higher plants

Igamberdiev, A. U., Popov, V. N., & Фалалеева, М. И. (1995) · FEBS Letters · doi:10.1016/0014-5793(95)00563-o · Cited by 24

Development of Antioxidant and Xenobiotic Metabolizing Enzyme Systems

Fanucchi, M. V. (2004) · Elsevier eBooks · doi:10.1016/b978-012324751-3/50046-2 · Cited by 24

Cerebellar superoxide dismutase expression in Menkes' kinky hair disease: an immunohistochemical investigation

Shibata, N., Hirano, A., Kobayashi, M., Umahara, T., Kawanami, T., & Asayama, K. (1995) · Acta Neuropathologica · doi:10.1007/bf00294321 · Cited by 24

Oxidative stress induction by Prunus necrotic ringspot virus infection in apricot seeds

Amari, K., Díaz‐Vivancos, P., Pallás, V., Sánchez‐Pina, M. A., & Hernández, J. A. (2007) · Physiologia Plantarum · doi:10.1111/j.1399-3054.2007.00961.x · Cited by 24

Environmental chemistry of reactive oxygen species

Larson, R. A., & McCord, J. M. (1977) · C R C Critical Reviews in Environmental Control · doi:10.1080/10643387709381663 · Cited by 23

Evaluation of negative staining technique for determination of CN−-insensitive superoxide dismutase activity

de Rosa, G., Duncan, D. S., Keen, C. L., & Hurley, L. S. (1979) · Biochimica et Biophysica Acta (BBA) - Enzymology · doi:10.1016/0005-2744(79)90245-6 · Cited by 24

Isolation and preliminary characterization of electrophoretic variants of copper, zinc superoxide dismutase

Civalleri, L., Pini, C., Rigo, A., Federico, R., Calabrese, L., & Rotilio, G. (1982) · Molecular and Cellular Biochemistry · doi:10.1007/bf00241560 · Cited by 24

Isolation and characterization of iron superoxide dismutase from Bacillus megaterium

Xuereb‐Anastasi, A., Bannister, J. V., & BANNISTER, W. H. (1976) · International Journal of Biochemistry · doi:10.1016/0020-711x(76)90072-0 · Cited by 24

Interspecific hybridisation in vitro of superoxide dismutase from various species

Tegelström, H. (2009) · Hereditas · doi:10.1111/j.1601-5223.1975.tb01033.x · Cited by 24

Cytosolic manganese superoxide dismutase genes from the white shrimp Litopenaeus vannamei are differentially expressed in response to lipopolysaccharides, white spot virus and during ontogeny

Gómez-Anduro, G. A., Ascencio‐Valle, F., Peregrino-Uriarte, A. B., Campa‐Córdova, Á. I., & Yepiz-Plascencia, G. M. (2012) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2012.03.003 · Cited by 25

Cu,Zn superoxide dismutase from Trematomus bernacchii: Functional conservation and erratic molecular evolution in Antarctic teleosts

Santovito, G., Cassini, A., & Piccinni, E. (2006) · Comparative Biochemistry and Physiology Part C Toxicology & Pharmacology · doi:10.1016/j.cbpc.2006.04.007 · Cited by 24

Concentration/activity of superoxide dismutase isozymes and the pro-/antioxidative status, in context of type 2 diabetes and selected single nucleotide polymorphisms (genes: INS, SOD1, SOD2, SOD3) - Preliminary findings.

Lewandowski, Ł., Urbanowicz, I., Kepinska, M., & Milnerowicz, H. (2021) · Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · doi:10.1016/j.biopha.2021.111396 · Cited by 19

Manganese superoxide dismutase is required to maintain osteoclast differentiation and function under static force

Guo, T., Zhang, L., Konermann, A., Zhou, H., Jin, F., & Liu, W. (2015) · Scientific Reports · doi:10.1038/srep08016 · Cited by 23

Acute cobalt exposure and oxygen radical scavengers in the rat myocardium

Hatori, N., Pehrsson, K., Clyne, N., Hansson, G. I., Hofman‐Bang, C., Marklund, S. L., Rydén, L., Sjöqvist, P.-O., & Svensso, L. (1993) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/0925-4439(93)90029-z · Cited by 23

Characteristics of plasma extracellular SOD in burned patients

Saitoh, D., Ookawara, T., Fukuzuka, K., Kawakami, M., Sakamoto, T., Ohno, H., & Okada, Y. (2001) · Burns · doi:10.1016/s0305-4179(01)00022-5 · Cited by 23

Expression of superoxide dismutase (SOD) in adenomyosis

Ishikawa, M., Nakata, T., Yaginuma, Y., 西脇, 邦., Goishi, K., & Saitoh, S. (1993) · American Journal of Obstetrics and Gynecology · doi:10.1016/0002-9378(93)90653-z · Cited by 23

Purification of Cu-Zn-superoxide dismutase from human erythrocytes by immunoaffinity chromatography Evidence for the presence of isoelectric heterogeneity

Arai, K., Iizuka, S., Makita, A., Oikawa, K., & Taniguchi, N. (1986) · Journal of Immunological Methods · doi:10.1016/0022-1759(86)90112-2 · Cited by 23

Increase in superoxide dismutase activity induced by thyroid hormones in the brains of neonate and adult rats

Petrović, V. M., Spasić, M. B., Saičić, Z. S., Milić, B., & Radojičić, R. (1982) · Cellular and Molecular Life Sciences · doi:10.1007/bf01954949 · Cited by 23

THE SUPEROXIDE ANION AS ELECTRON DONOR TO THE MITOCHONDRIAL ELECTRON TRANSPORT CHAIN

Ninnemann, H., Strasser, R. J., & Butler, W. L. (1977) · Photochemistry and Photobiology · doi:10.1111/j.1751-1097.1977.tb07446.x · Cited by 23

SOD2-Mediated Effects Induced by WR1065 and Low-Dose Ionizing Radiation on Micronucleus Formation in RKO Human Colon Carcinoma Cells

Murley, J. S., Kataoka, Y., Miller, R. C., Li, J. J., Woloschak, G. E., & Grdina, D. J. (2010) · Radiation Research · doi:10.1667/rr2349.1 · Cited by 22

Experimental and Computational Study of the Antioxidative Potential of Novel Nitro and Amino Substituted Benzimidazole/Benzothiazole-2-Carboxamides with Antiproliferative Activity

Cindrić, M., Sović, I., Mioč, M., Hok, L., Boček, I., Roškarić, P., Butković, K., Martin‐Kleiner, I., Starčević, K., Vianello, R., et al. (2019) · Antioxidants · doi:10.3390/antiox8100477 · Cited by 22

Purification and characterization of Cu, Zn-superoxide dismutase from black soybean

Wang, S., Shao, B., Liu, S., Ye, X., & Rao, P. (2011) · Food Research International · doi:10.1016/j.foodres.2011.10.023 · Cited by 22

Redox Regulation of the Superoxide Dismutases SOD3 and SOD2 in the Pulmonary Circulation

Hernández-Saavedra, D., Swain, K. E., Tuder, R. M., Petersen, S. V., & Nozik‐Grayck, E. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-63245-2_5 · Cited by 22

Dietary superoxide dismutase does not affect tissue levels

Zidenberg‐Cherr, S., Keen, C. L., Lönnerdal, B. L., & Hurley, L. S. (1983) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/37.1.5 · Cited by 22

Purification, N-terminal amino acid sequence, and some properties of Cu, Zn-superoxide dismutase from Japanese flounder (Paralichthys olivaceus) hepato-pancreas

Osatomi, K., Masuda, Y., Hara, K., & Ishihara, T. (2001) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/s1096-4959(01)00299-8 · Cited by 22

A Superoxide Dismutase Purified from the Rhizome of Curcuma aeruginosa Roxb. as Inhibitor of Nitric Oxide Production in the Macrophage-like RAW 264.7 Cell Line

Moon-ai, W., Niyomploy, P., Boonsombat, R., Sangvanich, P., & Karnchanatat, A. (2012) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-012-9640-9 · Cited by 22

Cloned Prokaryotic Iron Superoxide Dismutase Protects Yeast Cells against Oxidative Stress Depending on Mitochondrial Location

Balzan, R., Agius, D., & Bannister, W. H. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.0285 · Cited by 22

Overexpressions of myoglobin and antioxidant enzymes in ragged‐red fibers of skeletal muscle from patients with mitochondrial encephalomyopathy

Kunishige, M., Mitsui, T., Akaike, M., Kawajiri, M., Shono, M., Kawai, H., & Matsumoto, T. (2003) · Muscle & Nerve · doi:10.1002/mus.10466 · Cited by 22

Manganese superoxide dismutases from Escherichia coli and from yeast mitochondria: Preliminary X-ray crystallographic studies

Beem, K. M., Richardson, J. S., & Richardson, D. C. (1976) · Journal of Molecular Biology · doi:10.1016/0022-2836(76)90115-7 · Cited by 22

Purification et étude des deux superoxyde dismutases du champignon Pleurotus olearius

Lavelle, F., & Michelson, A. M. (1975) · Biochimie · doi:10.1016/s0300-9084(75)80314-2 · Cited by 22

Oxygen toxicity in normal and neoplastic hamster cells in culture

Goetz, I. E. (1975) · In Vitro Cellular & Developmental Biology - Plant · doi:10.1007/bf02616375 · Cited by 22

Reprint of: Generation of Superoxide Radical during Autoxidation of Hydroxylamine and an Assay for Superoxide Dismutase

Kono, Y. (2022) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2022.109247 · Cited by 21

Inhibition of Enzymes Involved in Neurodegenerative Disorders and Aβ1–40 Aggregation by Citrus limon Peel Polyphenol Extract

Arcone, R., D’Errico, A., Nasso, R., Rullo, R., Poli, A., Donato, P. D., & Masullo, M. (2023) · Molecules · doi:10.3390/molecules28176332 · Cited by 22

Purification, molecular cloning, and some properties of a manganese-containing superoxide dismutase from Japanese flounder (Paralichthys olivaceus)

Wang, Y., Osatomi, K., Nagatomo, Y., Yoshida, A., & Hara, K. (2011) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2010.12.007 · Cited by 21

Biochemical and molecular changes mediated by plasticizer diethyl phthalate in Chironomus circumdatus (bloodworms)

Shaha, C. M., & Pandit, R. S. (2019) · Comparative Biochemistry and Physiology Part C Toxicology & Pharmacology · doi:10.1016/j.cbpc.2019.108650 · Cited by 21

tert -Butyl- p -benzoquinone induces autophagy by inhibiting the Akt/mTOR signaling pathway in RAW 264.7 cells

Meng, X., Xia, C., Ye, Q., & Nie, X. (2020) · Food & Function · doi:10.1039/d0fo00281j · Cited by 21

Mitochondrial function is impaired in the primary visual cortex in an experimental glaucoma model

Arana, A. G. H., Vitar, R. M. L., Reides, C. G., Calabró, V., Marchini, T., Lerner, S. F., Evelson, P., & Ferreira, S. M. (2021) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2021.108815 · Cited by 21

C/EBPβ regulates TNF induced MnSOD expression and protection against apoptosis

Ranjan, P., & Boss, J. M. (2006) · APOPTOSIS · doi:10.1007/s10495-006-9530-0 · Cited by 21

Expression analysis and mitochondrial targeting properties of the chicken manganese-containing superoxide dismutase

Kong, B. C., Kim, H., & Foster, D. N. (2003) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/s0167-4781(02)00593-6 · Cited by 21

The effect of l-deprenyl, d-deprenyl and MDL72974 on mitochondrial respiration: a possible mechanism leading to an adaptive increase in superoxide dismutase activity

Thiffault, C., Quirion, R., & Poirier, J. (1997) · Molecular Brain Research · doi:10.1016/s0169-328x(97)00135-6 · Cited by 21

Tris(picolinato)manganese(II): a chemical model for the mechanism and function of mitochondrial superoxide dismutase

Yamaguchi, K. S., Spencer, L., & Sawyer, D. T. (1986) · FEBS Letters · doi:10.1016/0014-5793(86)80336-2 · Cited by 21

Biosynthesis and Cellular Distribution of the Two Superoxide Dismutases of Dactylium dendroides

Shatzman, A. R., & Kosman, D. J. (1979) · Journal of Bacteriology · doi:10.1128/jb.137.1.313-320.1979 · Cited by 21

Effect of Level of Dietary Protein and Total or Partial Starvation on Catalase and Superoxide Dismutase Activity in Cardiac and Skeletal Muscles in Young Rats

Lammi‐Keefe, C. J., Swan, P. B., & Hegarty, P. V. J. (1984) · Journal of Nutrition · doi:10.1093/jn/114.12.2235 · Cited by 21

A Manganese-containing superoxide dismutase from Paracoccus denitrificans

Terech, A., & Vignais, P. M. (1981) · Biochimica et Biophysica Acta (BBA) - Enzymology · doi:10.1016/0005-2744(81)90327-2 · Cited by 21

In vivo antioxidant potentials of rambutan, mangosteen, and langsat peel extracts and effects on liver enzymes in experimental rats

Samuagam, L., Sia, C. M., Akowuah, G. A., Okechukwu, P. N., & Yim, H. S. (2015) · Food Science and Biotechnology · doi:10.1007/s10068-015-0026-y · Cited by 20

The Basics of Oxidative Biochemistry

Miwa, S., Müller, F. L., & Beckman, K. B. (2008) · Humana Press eBooks · doi:10.1007/978-1-59745-420-9_2 · Cited by 20

The effect of aging and increasing ascorbate concentrations on respiratory chain activity in cultured human fibroblasts

Ghneim, H. K., & Al‐Sheikh, Y. A. (2010) · Cell Biochemistry and Function · doi:10.1002/cbf.1653 · Cited by 20

Superoxide dismutase protects ribonucleotide reductase from inactivation in yeast

Das, A. B., Sadowska‐Bartosz, I., Königstorfer, A., Kettle, A. J., & Winterbourn, C. C. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.01.001 · Cited by 20

Isolation and Properties of Superoxide Dismutase from Bovine Spermatozoa1

Magnes, L. J., & Li, T. (1980) · Biology of Reproduction · doi:10.1095/biolreprod22.4.965 · Cited by 20

Occurrence and distribution of antioxidant enzymes in the haemolymph of the shore crab Carcinus maenas

Bell, K. L., & Smith, V. J. (1995) · Marine Biology · doi:10.1007/bf00349127 · Cited by 20

Modulation of benzene toxicity by an interferon inducer (6MFA)

Pandya, K. P., Shanker, R., Gupta, A., Khan, W. A., & Ray, P. K. (1986) · Toxicology · doi:10.1016/0300-483x(86)90029-6 · Cited by 20

Superoxide dismutase specific activities in cultured human diploid cells of various donor ages

Duncan, M. R., Dell’Orco, R. T., & Kirk, K.-A. (1979) · Journal of Cellular Physiology · doi:10.1002/jcp.1040980219 · Cited by 20

Evidence for manganese(III) binding to the mangano superoxide dismutase from a higher plant (Pisum sativum L.)

Fernández, V. M., Sevilla, F., Lopez-Gorge, J., & del Río, L. A. (1982) · Journal of Inorganic Biochemistry · doi:10.1016/s0162-0134(00)80247-0 · Cited by 20

Superoxide dismutase and catalase activities in Ataxia telangiectasia and normal fibroblast cell extracts

Sheridan, R. B., & Huang, P. C. (1979) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/0027-5107(79)90141-6 · Cited by 20

Investigations into combined dietary deficiencies of copper, selenium, and vitamin E in the rat

Paynter, D. I., & Martin, G. B. (1980) · Biological Trace Element Research · doi:10.1007/bf02785353 · Cited by 20

Contribution to subcellular localization of superoxide dismutase isoforms of spruce needles and oak leaves

Sehmer, L., & Dizengremel, P. (1998) · Journal of Plant Physiology · doi:10.1016/s0176-1617(98)80202-2 · Cited by 19

Tissue Expression of Manganese Superoxide Dismutase Is a Candidate Prognostic Marker for Glioblastoma

Park, C., Jung, J. H., Moon, M. J., Kim, Y.-Y., Kim, J. H., Park, S., Kim, C., Paek, S. H., Kim, D. G., Jung, H., et al. (2009) · Oncology · doi:10.1159/000231888 · Cited by 19

Potential use of hirudin in diabetic cataract: A study of galactose mediated human lens epithelial cells injury

Ou, Y., Liao, G., & Wu-tong, W. (2008) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2008.02.012 · Cited by 19

Increased expression of manganese superoxide dismutase is associated with that of nitrotyrosine in myopathies with rimmed vacuoles

Tsuruta, Y., Furuta, A., Taniguchi, N., Yamada, T., Kira, J., & Iwaki, T. (2001) · Acta Neuropathologica · doi:10.1007/s004010100428 · Cited by 19

cDNA cloning, high-level expression, purification, and characterization of an avian Cu,Zn superoxide dismutase from Peking duck

Liu, W., Zhu, R.-H., Li, G., & Wang, D. (2002) · Protein Expression and Purification · doi:10.1016/s1046-5928(02)00040-2 · Cited by 19

Superoxide dismutase activity in the skin of rats irradiated by He-Ne laser

Parlato, G., Cimmino, G., Vendittis, E. D., Monfrecola, G., & Bocchini, V. (1983) · Cellular and Molecular Life Sciences · doi:10.1007/bf01990307 · Cited by 19

Age-associated cellular relocation of Sod 1 as a self-defense is a futile mechanism to prevent vascular aging

van der Loo, B., Bachschmid, M. M., Skepper, J. N., Labugger, R., Schildknecht, S., Hahn, R., Muessig, E., Gygi, D., & Lüscher, T. F. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.03.224 · Cited by 19

Toxic effects of ozone on human cells in vitro, exposed by gas diffusion through teflon film

Alink, G. M., Boer, R. M. D., Mol, J., & Temmink, J. H. M. (1980) · Toxicology · doi:10.1016/0300-483x(80)90096-7 · Cited by 19

Oxidative stress in organ preservation: a multifaceted approach to cardioplegia

Nelson, S. K., Bose, S. K., Rizeq, M. N., & McCord, J. M. (2005) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2005.03.007 · Cited by 19

Factor Analysis of the Activities of Superoxide Dismutase, Catalase and Glutathione Peroxidase in Normal Tissues and Neoplastic Cell Lines

BANNISTER, W. H., & Bannister, J. V. (1987) · Free Radical Research Communications · doi:10.3109/10715768709088082 · Cited by 19

Effect of nickel chloride on streptozotocin-induced diabetes in rats

Novelli, E. L. B., Rodrigues, N. L., & Ribas, B. O. (1988) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/y88-104 · Cited by 19

Gene Affecting Superoxide Dismutase Activity Linked to the Histocompatibility Complex in H-2 Congenic Mice

NOVAK, R. F., Bösze, Z., Matkovics, B., & Fachet, J. (1980) · Science · doi:10.1126/science.7350646 · Cited by 19

Accumulation of low molecular weight (bleomycin detectable) iron in bone marrow cells of rats after benzene exposure

Pandya, K. P., Rao, G. S., Khan, S. G., & Krishnamurthy, R. (1990) · Archives of Toxicology · doi:10.1007/bf01972997 · Cited by 19

Oxygen Utilization and Toxicity in the Lungs

Fisher, A. B., & Forman, H. J. (1985) · Comprehensive physiology · doi:10.1002/cphy.cp030105 · Cited by 19

Characterization, antimicrobial and antitumor activity of superoxide dismutase extracted from Egyptian honeybee venom (Apis mellifera lamarckii)

Abdel-Monsef, M. M., Darwish, D. A., Zidan, H. A., Hamed, A. A., & Ibrahim, M. A.-A. (2023) · Journal of Genetic Engineering and Biotechnology · doi:10.1186/s43141-023-00470-4 · Cited by 18

Identification of Superoxide Dismutase (SOD) Isozymes in Plant Tissues

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Fanucchi, M. V. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-799941-8.00011-0 · Cited by 21

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Allgood, G. S., & Perry, J. J. (1985) · Canadian Journal of Microbiology · doi:10.1139/m85-190 · Cited by 18

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Saito, T., Kurasaki, M., Kaji, H., & Saito, K. (1984) · Cancer Letters · doi:10.1016/0304-3835(84)90129-0 · Cited by 18

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